Protease-mediated degradation of lignin peroxidase in liquid cultures of Phanerochaete chrysosporium.
Identifieur interne : 000F40 ( Main/Exploration ); précédent : 000F39; suivant : 000F41Protease-mediated degradation of lignin peroxidase in liquid cultures of Phanerochaete chrysosporium.
Auteurs : C G Dosoretz [États-Unis] ; S B Dass ; C A Reddy ; H E GrethleinSource :
- Applied and environmental microbiology [ 0099-2240 ] ; 1990.
Descripteurs français
- KwdFr :
- Basidiomycota (effets des médicaments et des substances chimiques), Basidiomycota (métabolisme), Cinétique (MeSH), Endopeptidases (métabolisme), Glucose (métabolisme), Glucose (pharmacologie), Isoenzymes (antagonistes et inhibiteurs), Isoenzymes (métabolisme), Lignine (métabolisme), Peroxidases (antagonistes et inhibiteurs), Peroxidases (métabolisme).
- MESH :
- antagonistes et inhibiteurs : Isoenzymes, Peroxidases.
- effets des médicaments et des substances chimiques : Basidiomycota.
- métabolisme : Basidiomycota, Endopeptidases, Glucose, Isoenzymes, Lignine, Peroxidases.
- pharmacologie : Glucose.
- Cinétique.
English descriptors
- KwdEn :
- Basidiomycota (drug effects), Basidiomycota (metabolism), Endopeptidases (metabolism), Glucose (metabolism), Glucose (pharmacology), Isoenzymes (antagonists & inhibitors), Isoenzymes (metabolism), Kinetics (MeSH), Lignin (metabolism), Peroxidases (antagonists & inhibitors), Peroxidases (metabolism).
- MESH :
- chemical , antagonists & inhibitors : Isoenzymes, Peroxidases.
- chemical , metabolism : Endopeptidases, Glucose, Isoenzymes, Lignin, Peroxidases.
- drug effects : Basidiomycota.
- metabolism : Basidiomycota.
- chemical , pharmacology : Glucose.
- Kinetics.
Abstract
The decline of lignin peroxidase (LiP) activity observed after day 6 in cultures of Phanerochaete chrysosporium was found to be correlated with the appearance of idiophasic extracellular protease activity. Daily addition of glucose started on day 6 resulted in low protease levels and in turn in stable LiP levels. Addition of cycloheximide to day 6 cultures resulted in virtually no change of LiP activity and extracellular protein and negligible levels of protease activity, indicating that this protease is synthesized de novo. LiP activity was found to be stable upon removal of the fungal pellets on day 6 and incubation of the extracellular fluid alone. An almost complete disappearance of LiP activity and LiP proteins and high levels of protease activity were observed upon incubation of 6-day extracellular fluid in the presence of fungal pellets. Moreover, incubation of crude or purified LiP isoenzymes with protease-rich extracellular fluid of day 11 or 11-day cell extracts resulted in a marked loss of activity. In contrast, incubation of crude LiP with boiled and clarified extracellular fluid of day 11 cultures resulted in virtually no loss of activity. These results indicate that protease-mediated degradation of LiP proteins is a major cause for the decay of LiP activity during late secondary metabolism in cultures of P. chrysosporium.
DOI: 10.1128/AEM.56.11.3429-3434.1990
PubMed: 2268154
PubMed Central: PMC184972
Affiliations:
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scheme="KwdEn" xml:lang="en"><term>Basidiomycota (drug effects)</term><term>Basidiomycota (metabolism)</term><term>Endopeptidases (metabolism)</term><term>Glucose (metabolism)</term><term>Glucose (pharmacology)</term><term>Isoenzymes (antagonists & inhibitors)</term><term>Isoenzymes (metabolism)</term><term>Kinetics (MeSH)</term><term>Lignin (metabolism)</term><term>Peroxidases (antagonists & inhibitors)</term><term>Peroxidases (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Basidiomycota (effets des médicaments et des substances chimiques)</term><term>Basidiomycota (métabolisme)</term><term>Cinétique (MeSH)</term><term>Endopeptidases (métabolisme)</term><term>Glucose (métabolisme)</term><term>Glucose (pharmacologie)</term><term>Isoenzymes (antagonistes et inhibiteurs)</term><term>Isoenzymes (métabolisme)</term><term>Lignine (métabolisme)</term><term>Peroxidases (antagonistes et inhibiteurs)</term><term>Peroxidases (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Isoenzymes</term><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Endopeptidases</term><term>Glucose</term><term>Isoenzymes</term><term>Lignin</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Isoenzymes</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Basidiomycota</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Basidiomycota</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Basidiomycota</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Basidiomycota</term><term>Endopeptidases</term><term>Glucose</term><term>Isoenzymes</term><term>Lignine</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Glucose</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Glucose</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Kinetics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The decline of lignin peroxidase (LiP) activity observed after day 6 in cultures of Phanerochaete chrysosporium was found to be correlated with the appearance of idiophasic extracellular protease activity. Daily addition of glucose started on day 6 resulted in low protease levels and in turn in stable LiP levels. Addition of cycloheximide to day 6 cultures resulted in virtually no change of LiP activity and extracellular protein and negligible levels of protease activity, indicating that this protease is synthesized de novo. LiP activity was found to be stable upon removal of the fungal pellets on day 6 and incubation of the extracellular fluid alone. An almost complete disappearance of LiP activity and LiP proteins and high levels of protease activity were observed upon incubation of 6-day extracellular fluid in the presence of fungal pellets. Moreover, incubation of crude or purified LiP isoenzymes with protease-rich extracellular fluid of day 11 or 11-day cell extracts resulted in a marked loss of activity. In contrast, incubation of crude LiP with boiled and clarified extracellular fluid of day 11 cultures resulted in virtually no loss of activity. These results indicate that protease-mediated degradation of LiP proteins is a major cause for the decay of LiP activity during late secondary metabolism in cultures of P. chrysosporium.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">2268154</PMID><DateCompleted><Year>1991</Year><Month>02</Month><Day>08</Day></DateCompleted><DateRevised><Year>2020</Year><Month>07</Month><Day>24</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0099-2240</ISSN><JournalIssue CitedMedium="Print"><Volume>56</Volume><Issue>11</Issue><PubDate><Year>1990</Year><Month>Nov</Month></PubDate></JournalIssue><Title>Applied and environmental microbiology</Title><ISOAbbreviation>Appl Environ Microbiol</ISOAbbreviation></Journal><ArticleTitle>Protease-mediated degradation of lignin peroxidase in liquid cultures of Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>3429-34</MedlinePgn></Pagination><Abstract><AbstractText>The decline of lignin peroxidase (LiP) activity observed after day 6 in cultures of Phanerochaete chrysosporium was found to be correlated with the appearance of idiophasic extracellular protease activity. Daily addition of glucose started on day 6 resulted in low protease levels and in turn in stable LiP levels. Addition of cycloheximide to day 6 cultures resulted in virtually no change of LiP activity and extracellular protein and negligible levels of protease activity, indicating that this protease is synthesized de novo. LiP activity was found to be stable upon removal of the fungal pellets on day 6 and incubation of the extracellular fluid alone. An almost complete disappearance of LiP activity and LiP proteins and high levels of protease activity were observed upon incubation of 6-day extracellular fluid in the presence of fungal pellets. Moreover, incubation of crude or purified LiP isoenzymes with protease-rich extracellular fluid of day 11 or 11-day cell extracts resulted in a marked loss of activity. In contrast, incubation of crude LiP with boiled and clarified extracellular fluid of day 11 cultures resulted in virtually no loss of activity. These results indicate that protease-mediated degradation of LiP proteins is a major cause for the decay of LiP activity during late secondary metabolism in cultures of P. chrysosporium.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Dosoretz</LastName><ForeName>C G</ForeName><Initials>CG</Initials><AffiliationInfo><Affiliation>Department of Chemical Engineering, Michigan State University, East Lansing 48824.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dass</LastName><ForeName>S B</ForeName><Initials>SB</Initials></Author><Author ValidYN="Y"><LastName>Reddy</LastName><ForeName>C A</ForeName><Initials>CA</Initials></Author><Author ValidYN="Y"><LastName>Grethlein</LastName><ForeName>H E</ForeName><Initials>HE</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>1RO1 GM39032-01</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United 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1.11.1.-</RegistryNumber><NameOfSubstance UI="C042858">lignin peroxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.-</RegistryNumber><NameOfSubstance UI="D010450">Endopeptidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>IY9XDZ35W2</RegistryNumber><NameOfSubstance UI="D005947">Glucose</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001487" MajorTopicYN="N">Basidiomycota</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010450" MajorTopicYN="N">Endopeptidases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005947" MajorTopicYN="N">Glucose</DescriptorName><QualifierName UI="Q000378" 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PubStatus="pubmed"><Year>1990</Year><Month>11</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1990</Year><Month>11</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1990</Year><Month>11</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">2268154</ArticleId><ArticleId IdType="pmc">PMC184972</ArticleId><ArticleId IdType="doi">10.1128/AEM.56.11.3429-3434.1990</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Biochem Biophys Res Commun. 1983 Aug 12;114(3):1077-83</Citation><ArticleIdList><ArticleId IdType="pubmed">6615503</ArticleId></ArticleIdList></Reference><Reference><Citation>Crit Rev Microbiol. 1987;15(2):141-68</Citation><ArticleIdList><ArticleId IdType="pubmed">3322681</ArticleId></ArticleIdList></Reference><Reference><Citation>Appl Environ Microbiol. 1990 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IdType="pubmed">2760033</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Michigan</li></region><settlement><li>East Lansing</li></settlement><orgName><li>Université d'État du Michigan</li></orgName></list><tree><noCountry><name sortKey="Dass, S B" sort="Dass, S B" uniqKey="Dass S" first="S B" last="Dass">S B Dass</name><name sortKey="Grethlein, H E" sort="Grethlein, H E" uniqKey="Grethlein H" first="H E" last="Grethlein">H E Grethlein</name><name sortKey="Reddy, C A" sort="Reddy, C A" uniqKey="Reddy C" first="C A" last="Reddy">C A Reddy</name></noCountry><country name="États-Unis"><region name="Michigan"><name sortKey="Dosoretz, C G" sort="Dosoretz, C G" uniqKey="Dosoretz C" first="C G" last="Dosoretz">C G Dosoretz</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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